메뉴 건너뛰기




Volumn 51, Issue 4, 2010, Pages 327-333

Characterization of Hlcyst-3 as a member of cystatins from the tick Haemaphysalis longicornis

Author keywords

Cystatin; Haemaphysalis longicornis; Hlcyst 3

Indexed keywords

CATHEPSIN L; CYSTATIN; ENZYME INHIBITOR; PAPAIN; RECOMBINANT PROTEIN;

EID: 77954428098     PISSN: 01688162     EISSN: 15729702     Source Type: Journal    
DOI: 10.1007/s10493-010-9336-1     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 0030053568 scopus 로고    scopus 로고
    • A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: Purification, characterization, cDNA cloning, and tissue localization
    • Agarwala KL, Kawabata S, Hirata M, Miyagi M, Tsunasawa S, Iwanaga S (1996) A cysteine protease inhibitor stored in the large granules of horseshoe crab hemocytes: purification, characterization, cDNA cloning, and tissue localization. J Biochem 119: 85-94.
    • (1996) J Biochem , vol.119 , pp. 85-94
    • Agarwala, K.L.1    Kawabata, S.2    Hirata, M.3    Miyagi, M.4    Tsunasawa, S.5    Iwanaga, S.6
  • 2
    • 77954427991 scopus 로고    scopus 로고
    • Barrett AJ, Rawlings ND, Davies ME, Machleidt W, Salvesen G, Turk V (1986) In: Barret AJ, Salvesen G (Eds.) Cysteine proteinase inhibitors of the cystatin superfamily in protease inhibitors. Elsevier, New York, pp. 515-569.
  • 3
    • 0029776802 scopus 로고    scopus 로고
    • The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases
    • Bjork I, Brieditis I, Raub-Segall E, Pol E, Hakansson K, Abrahamson M (1996) The importance of the second hairpin loop of cystatin C for proteinase binding. Characterization of the interaction of Trp-106 variants of the inhibitor with cysteine proteinases. Biochemistry 35: 10720-10726.
    • (1996) Biochemistry , vol.35 , pp. 10720-10726
    • Bjork, I.1    Brieditis, I.2    Raub-Segall, E.3    Pol, E.4    Hakansson, K.5    Abrahamson, M.6
  • 4
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-New members and their evolution
    • Brown WM, Dziegielewska KM (1997) Friends and relations of the cystatin superfamily-New members and their evolution. Protein Sci 6: 5-12.
    • (1997) Protein Sci , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 5
    • 0035190790 scopus 로고    scopus 로고
    • Nippocystatin, a cysteine protease inhibitor from Nippostrongylus brasiliensis, inhibits antigen processing and modulates antigen-specific immune response
    • Dainichi T, Maekawa Y, Ishii K, Zhang T, Nashed BF, Sakai T, Takashima M, Himeno K (2001) Nippocystatin, a cysteine protease inhibitor from Nippostrongylus brasiliensis, inhibits antigen processing and modulates antigen-specific immune response. Infect Immun 69: 7380-7386.
    • (2001) Infect Immun , vol.69 , pp. 7380-7386
    • Dainichi, T.1    Maekawa, Y.2    Ishii, K.3    Zhang, T.4    Nashed, B.F.5    Sakai, T.6    Takashima, M.7    Himeno, K.8
  • 6
    • 33745705739 scopus 로고
    • Structure and expression of the gene encoding cystatin D, a novel human cysteine inhibitor interaction
    • Frejie JP, Abrahamson M, Olafssonn I, Velasco G, Grubb A, Lopez-Otin C (1991) Structure and expression of the gene encoding cystatin D, a novel human cysteine inhibitor interaction. EMBO J 9: 1939-1947.
    • (1991) EMBO J , vol.9 , pp. 1939-1947
    • Frejie, J.P.1    Abrahamson, M.2    Olafssonn, I.3    Velasco, G.4    Grubb, A.5    Lopez-Otin, C.6
  • 7
    • 0017943792 scopus 로고
    • Development of acquired resistance and precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: Ixodidae)
    • Fujisaki K (1978) Development of acquired resistance and precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: Ixodidae). Natl Inst Anim Health Quart (Tokyo) 18: 27-38.
    • (1978) Natl Inst Anim Health Quart (Tokyo) , vol.18 , pp. 27-38
    • Fujisaki, K.1
  • 8
    • 0028366341 scopus 로고
    • The taxonomy of the bovine Theileria spp
    • Fujisaki K, Kawazu S, Kamio T (1994) The taxonomy of the bovine Theileria spp. Parasitol Today 10: 31-33.
    • (1994) Parasitol Today , vol.10 , pp. 31-33
    • Fujisaki, K.1    Kawazu, S.2    Kamio, T.3
  • 9
    • 0037067236 scopus 로고    scopus 로고
    • Genes encoding two cystatins in the flesh fly Sarcophaga crassipalpis and their distinct expression patterns in relation to pupal diapause
    • Goto SG, Denlinger DL (2002) Genes encoding two cystatins in the flesh fly Sarcophaga crassipalpis and their distinct expression patterns in relation to pupal diapause. Gene 292: 121-127.
    • (2002) Gene , vol.292 , pp. 121-127
    • Goto, S.G.1    Denlinger, D.L.2
  • 10
    • 33751538306 scopus 로고    scopus 로고
    • Two secreted cystatins of the soft tick Ornithodoros moubata: Differential expression pattern and inhibitory specificity
    • Grunclova L, Horn M, Vancova M, Sojka D, Franta Z, Mares M, Kopacek P (2006) Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity. Biol Chem 387: 1635-1644.
    • (2006) Biol Chem , vol.387 , pp. 1635-1644
    • Grunclova, L.1    Horn, M.2    Vancova, M.3    Sojka, D.4    Franta, Z.5    Mares, M.6    Kopacek, P.7
  • 11
    • 16844371922 scopus 로고    scopus 로고
    • The global importance of ticks
    • Jongejan F, Uilenberg G (2004) The global importance of ticks. Parasitology 129: S3-S14.
    • (2004) Parasitology , vol.129 , pp. 3-14
    • Jongejan, F.1    Uilenberg, G.2
  • 12
    • 23044433357 scopus 로고    scopus 로고
    • RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding
    • Karim S, Miller NJ, Valenzuela J, Sauer JR, Mather TN (2005) RNAi-mediated gene silencing to assess the role of synaptobrevin and cystatin in tick blood feeding. Biochem Biophys Res Commu 334: 1336-1342.
    • (2005) Biochem Biophys Res Commu , vol.334 , pp. 1336-1342
    • Karim, S.1    Miller, N.J.2    Valenzuela, J.3    Sauer, J.R.4    Mather, T.N.5
  • 13
    • 33748746599 scopus 로고    scopus 로고
    • Anti-inflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis
    • Kotsyfakis M, Sa-Nunes A, Francischetti IM, Mather TN, Andersen JF, Ribeiro JM (2006) Anti-inflammatory and immunosuppressive activity of sialostatin L, a salivary cystatin from the tick Ixodes scapularis. J Biol Chem 281: 26298-26307.
    • (2006) J Biol Chem , vol.281 , pp. 26298-26307
    • Kotsyfakis, M.1    Sa-Nunes, A.2    Francischetti, I.M.3    Mather, T.N.4    Andersen, J.F.5    Ribeiro, J.M.6
  • 14
    • 35748942888 scopus 로고    scopus 로고
    • Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis
    • Kotsyfakis M, Karim S, Andersen JF, Mather TN, Ribeiro JM (2007) Selective cysteine protease inhibition contributes to blood-feeding success of the tick Ixodes scapularis. J Biol Chem 282: 29256-29263.
    • (2007) J Biol Chem , vol.282 , pp. 29256-29263
    • Kotsyfakis, M.1    Karim, S.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 15
    • 33745746366 scopus 로고    scopus 로고
    • Bmcystatin, a cysteine proteinase inhibitor characterized from the tick Boophilus microplus
    • Lima CA, Sasaki SD, Tanaka AS (2006) Bmcystatin, a cysteine proteinase inhibitor characterized from the tick Boophilus microplus. Biochem Biophys Res Commun 347: 44-50.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 44-50
    • Lima, C.A.1    Sasaki, S.D.2    Tanaka, A.S.3
  • 16
    • 0035916803 scopus 로고    scopus 로고
    • Bm-CPI- 2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing
    • Manoury B, Gregory WF, Maizels RM, Watts C (2001) Bm-CPI- 2, a cystatin homolog secreted by the filarial parasite Brugia malayi, inhibits class II MHC-restricted antigen processing. Curr Biol 11: 447-451.
    • (2001) Curr Biol , vol.11 , pp. 447-451
    • Manoury, B.1    Gregory, W.F.2    Maizels, R.M.3    Watts, C.4
  • 17
    • 0033128927 scopus 로고    scopus 로고
    • Molecular cloning of two Haemaphysalis longicornis. Cathepsin L-like cysteine proteinase genes
    • Mulenga A, Sugimoto C, Ingram G, Ohashi K, Onuma M (1999) Molecular cloning of two Haemaphysalis longicornis. Cathepsin L-like cysteine proteinase genes. J Vet Med Sci 61: 497-503.
    • (1999) J Vet Med Sci , vol.61 , pp. 497-503
    • Mulenga, A.1    Sugimoto, C.2    Ingram, G.3    Ohashi, K.4    Onuma, M.5
  • 18
    • 0025022426 scopus 로고
    • Evolution of proteins of the cystatin superfamily
    • Rawlings ND, Barrett AJ (1990) Evolution of proteins of the cystatin superfamily. J Mol Evol 30: 60-71.
    • (1990) J Mol Evol , vol.30 , pp. 60-71
    • Rawlings, N.D.1    Barrett, A.J.2
  • 20
    • 44949197678 scopus 로고    scopus 로고
    • A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks
    • Tsuji N, Miyoshi T, Battsetseg B, Matsuo T, Xuan X, Fujisaki K (2008) A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks. PLoS Pathog 16(4(5)): e1000062.
    • (2008) PLoS Pathog , vol.16 , Issue.4-5
    • Tsuji, N.1    Miyoshi, T.2    Battsetseg, B.3    Matsuo, T.4    Xuan, X.5    Fujisaki, K.6
  • 21
    • 0025817602 scopus 로고
    • The cystatins: Protein inhibitors of cysteine proteinases
    • Turk V, Bode W (1991) The cystatins: protein inhibitors of cysteine proteinases. Fed Eur Biol Soc Lett 285: 213-219.
    • (1991) Fed Eur Biol Soc Lett , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 22
    • 0033210951 scopus 로고    scopus 로고
    • Purification and characterization of Bombyx cysteine proteinase specific inhibitors from the hemolymph of Bombyx mori
    • Yamamoto Y, Watabe S, Kageyama T, Takahashi S (1999) Purification and characterization of Bombyx cysteine proteinase specific inhibitors from the hemolymph of Bombyx mori. Arch Insect Biochem Physiol 41: 119-129.
    • (1999) Arch Insect Biochem Physiol , vol.41 , pp. 119-129
    • Yamamoto, Y.1    Watabe, S.2    Kageyama, T.3    Takahashi, S.4
  • 23
    • 33745713839 scopus 로고    scopus 로고
    • A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity
    • Zhou J, Ueda M, Umemiya R, Battsetseg B, Boldbaatar D, Xuan X, Fujisaki K (2006) A secreted cystatin from the tick Haemaphysalis longicornis and its distinct expression patterns in relation to innate immunity. Insect Biochem Mol Biol 36: 527-535.
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 527-535
    • Zhou, J.1    Ueda, M.2    Umemiya, R.3    Battsetseg, B.4    Boldbaatar, D.5    Xuan, X.6    Fujisaki, K.7
  • 24
    • 59649083646 scopus 로고    scopus 로고
    • Characterization of an intracellular cystatin homolog from the tick Haemaphysalis longicornis
    • Zhou J, Liao M, Ueda M, Gong H, Xuan X, Fujisaki K (2009) Characterization of an intracellular cystatin homolog from the tick Haemaphysalis longicornis. Vet Parasitol 160: 180-183.
    • (2009) Vet Parasitol , vol.160 , pp. 180-183
    • Zhou, J.1    Liao, M.2    Ueda, M.3    Gong, H.4    Xuan, X.5    Fujisaki, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.